1AK1

FERROCHELATASE FROM BACILLUS SUBTILIS

Summary for 1AK1

• Entry DOI: 10.2210/pdb1ak1/pdb
• Descriptor: FERROCHELATASE (2 entities in total)
• Functional Keywords: protoheme ferro-lyase, heme synthesis, porphyrin, metallation, b. subtilis
• Biological source: Bacillus subtilis
• Cellular location: Cytoplasm: P32396
• Total number of polymer chains: 1
• Total formula weight: 35389.71

Authors

Al-Karadaghi, S.,Hansson, M.,Nikonov, S.,Jonsson, B.,Hederstedt, L. (deposition date: 1997-05-28, release date: 1997-12-03, Last modification date: 2024-02-07)

Primary citation

Al-Karadaghi, S.,Hansson, M.,Nikonov, S.,Jonsson, B.,Hederstedt, L.
Crystal structure of ferrochelatase: the terminal enzyme in heme biosynthesis.
Structure, 5:1501-1510, 1997

PubMed Abstract: The metallation of closed ring tetrapyrroles resulting in the formation of hemes, chlorophylls and vitamin B12 is catalyzed by specific enzymes called chelatases. Ferrochelatase catalyzes the terminal step in heme biosynthesis by inserting ferrous ion into protoporphyrin IX by a mechanism that is poorly understood. Mutations in the human gene for ferrochelatase can result in the disease erythropoietic protoporphyria, and a further understanding of the mechanism of this enzyme is therefore of clinical interest. No three-dimensional structure of a tetrapyrrole metallation enzyme has been available until now.

PubMed: 9384565
DOI: 10.1016/S0969-2126(97)00299-2

Experimental method

X-RAY DIFFRACTION (1.9 Å)